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Conserved domains on  [gi|445942851|ref|WP_000020706|]
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MULTISPECIES: chemotaxis protein CheA [Shigella]

Protein Classification

chemotaxis protein CheA( domain architecture ID 11484784)

chemotaxis protein CheA is a sensor histitine protein kinase that transmits sensory signals from chemoreceptors to the flagellar motors

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-654 0e+00

chemotaxis protein CheA; Provisional


:

Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1388.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   3 IDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547   1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  83 LNTDIINLFLETKDIMQEQLDAYKQSQEPDAASYDYICQALRQLALEAKGETPSAVTRLSVVAK---SEPQDEQSRSQLP 159
Cdd:PRK10547  81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIqekSEPQDESPRSQSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 160 RRIILSRLKAGEVDLLEEELGHLTTLNDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFET-------------- 225
Cdd:PRK10547 161 LRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETavaapqekaeette 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 226 -VEVSPKIATPPVLKLAAEQAPTGRVEREKTTRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLI 304
Cdd:PRK10547 241 vVEVSPKISVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 305 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 384
Cdd:PRK10547 321 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 385 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQ 464
Cdd:PRK10547 401 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPGFSTAEQ 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 465 VTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHP 544
Cdd:PRK10547 481 VTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREEDLHP 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 545 LAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 624
Cdd:PRK10547 561 LAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 640

                        650       660       670
                 ....*....|....*....|....*....|
gi 445942851 625 ILGDGSVALIVDVSALQAINREQRMANTAA 654
Cdd:PRK10547 641 ILGDGSVALIVDVSALQALNREQRMANTAA 670
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-654 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1388.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   3 IDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547   1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  83 LNTDIINLFLETKDIMQEQLDAYKQSQEPDAASYDYICQALRQLALEAKGETPSAVTRLSVVAK---SEPQDEQSRSQLP 159
Cdd:PRK10547  81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIqekSEPQDESPRSQSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 160 RRIILSRLKAGEVDLLEEELGHLTTLNDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFET-------------- 225
Cdd:PRK10547 161 LRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETavaapqekaeette 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 226 -VEVSPKIATPPVLKLAAEQAPTGRVEREKTTRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLI 304
Cdd:PRK10547 241 vVEVSPKISVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 305 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 384
Cdd:PRK10547 321 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 385 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQ 464
Cdd:PRK10547 401 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPGFSTAEQ 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 465 VTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHP 544
Cdd:PRK10547 481 VTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREEDLHP 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 545 LAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 624
Cdd:PRK10547 561 LAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 640

                        650       660       670
                 ....*....|....*....|....*....|
gi 445942851 625 ILGDGSVALIVDVSALQAINREQRMANTAA 654
Cdd:PRK10547 641 ILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-653 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 723.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   3 IDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQ 82
Cdd:COG0643    1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  83 LNTDIINLFLETKDIMQEQLDAYKQSQEPDAASYDyicqalrqlaleakgetpsavtrlsvvaksepqdeqsrsqlprri 162
Cdd:COG0643   81 LTPELIDLLLEALDALRALLDALEAGGEPPADISA--------------------------------------------- 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 163 ILSRLKAGEVDLLEeelghlttlndvvkgadslsailpgdiaedditavlcfvieadqITFETVEVSPKIATPPVLKlAA 242
Cdd:COG0643  116 LLARLDASEEAIEE--------------------------------------------VVADEVEISPPAPAALEPA-PA 150

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 243 EQAPTGRVEREKTTRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQESVM 322
Cdd:COG0643  151 AAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESLRELEEALEQLSRLTRELQDGVM 230

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 323 SIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGN 402
Cdd:COG0643  231 RLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGT 310

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 403 LILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSE---NMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVK 479
Cdd:COG0643  311 ITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEeaaALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVK 390

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 480 RNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHPLAGGErVLEVRGEYL 559
Cdd:COG0643  391 TNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGRE-VIRLRGELL 469

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 560 PIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSA 639
Cdd:COG0643  470 PLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAA 549

                        650
                 ....*....|....
gi 445942851 640 LQAINREQRMANTA 653
Cdd:COG0643  550 LVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 332-506 3.21e-95

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 290.64  E-value: 3.21e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 332 VFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQG 411
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 412 GNICIEVTDDGAGLNRERILAKAASQGLTVSE---NMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 488
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 445942851 489 VEIQSKQGTGTTIRILLP 506
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
502-640 1.00e-29

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 114.26  E-value: 1.00e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   502 RILLPLTLAILDgmsvrvaDEVFILPLNAVMESLQPREADL--HPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEAtQ 579
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942851   580 GIVVILQSGGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 640
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 514-640 2.95e-28

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 109.98  E-value: 2.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  514 GMSVRVADEVFILPLNAVMESLQPREADLHPLAGG--ERVLEVRGEYLPIVELWKVFNVAGAKTEaTQGIVVILQSGGRR 591
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 445942851  592 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 640
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-654 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1388.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   3 IDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQ 82
Cdd:PRK10547   1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  83 LNTDIINLFLETKDIMQEQLDAYKQSQEPDAASYDYICQALRQLALEAKGETPSAVTRLSVVAK---SEPQDEQSRSQLP 159
Cdd:PRK10547  81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIqekSEPQDESPRSQSG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 160 RRIILSRLKAGEVDLLEEELGHLTTLNDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFET-------------- 225
Cdd:PRK10547 161 LRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETavaapqekaeette 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 226 -VEVSPKIATPPVLKLAAEQAPTGRVEREKTTRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLI 304
Cdd:PRK10547 241 vVEVSPKISVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLI 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 305 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 384
Cdd:PRK10547 321 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 385 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQ 464
Cdd:PRK10547 401 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPGFSTAEQ 480

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 465 VTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHP 544
Cdd:PRK10547 481 VTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREEDLHP 560

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 545 LAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 624
Cdd:PRK10547 561 LAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAAT 640

                        650       660       670
                 ....*....|....*....|....*....|
gi 445942851 625 ILGDGSVALIVDVSALQAINREQRMANTAA 654
Cdd:PRK10547 641 ILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-653 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 723.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   3 IDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQ 82
Cdd:COG0643    1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  83 LNTDIINLFLETKDIMQEQLDAYKQSQEPDAASYDyicqalrqlaleakgetpsavtrlsvvaksepqdeqsrsqlprri 162
Cdd:COG0643   81 LTPELIDLLLEALDALRALLDALEAGGEPPADISA--------------------------------------------- 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 163 ILSRLKAGEVDLLEeelghlttlndvvkgadslsailpgdiaedditavlcfvieadqITFETVEVSPKIATPPVLKlAA 242
Cdd:COG0643  116 LLARLDASEEAIEE--------------------------------------------VVADEVEISPPAPAALEPA-PA 150

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 243 EQAPTGRVEREKTTRSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNHGDLITSMGQLQRNARDLQESVM 322
Cdd:COG0643  151 AAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESLRELEEALEQLSRLTRELQDGVM 230

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 323 SIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGN 402
Cdd:COG0643  231 RLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGT 310

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 403 LILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLTVSE---NMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVK 479
Cdd:COG0643  311 ITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEeaaALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVK 390

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 480 RNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREADLHPLAGGErVLEVRGEYL 559
Cdd:COG0643  391 TNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGRE-VIRLRGELL 469

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 560 PIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSA 639
Cdd:COG0643  470 PLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAA 549

                        650
                 ....*....|....
gi 445942851 640 LQAINREQRMANTA 653
Cdd:COG0643  550 LVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 332-506 3.21e-95

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 290.64  E-value: 3.21e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 332 VFSRYPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQG 411
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 412 GNICIEVTDDGAGLNRERILAKAASQGLTVSE---NMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 488
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 445942851 489 VEIQSKQGTGTTIRILLP 506
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 509-640 4.68e-54

CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. Activated by the chemotaxis receptor a histidine phosphoryl group from CheA is passed directly to an aspartate in the response regulator CheY. This signalling mechanism is modulated by the methyl accepting chemotaxis proteins (MCPs). MCPs form a highly interconnected, tightly packed array within the membrane that is organized, at least in part, through interactions with CheW and CheA. The CheA regulatory domain belongs to the family of CheW_like proteins and has been proposed to mediate interaction with the kinase regulator CheW.


Pssm-ID: 238373 [Multi-domain]  Cd Length: 132  Bit Score: 180.84  E-value: 4.68e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 509 LAILDGMSVRVADEVFILPLNAVMESLQPREADLHPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSG 588
Cdd:cd00731    1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEVINVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445942851 589 GRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSAL 640
Cdd:cd00731   81 GRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW smart00260
Two component signalling adaptor domain;
502-640 1.00e-29

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 114.26  E-value: 1.00e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   502 RILLPLTLAILDgmsvrvaDEVFILPLNAVMESLQPREADL--HPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEAtQ 579
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 445942851   580 GIVVILQSGGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 640
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 511-640 2.15e-29

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 238331  Cd Length: 136  Bit Score: 113.14  E-value: 2.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 511 ILDGMSVRVADEVFILPLNAVMESLQPREADLHPLA--GGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSG 588
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNApdYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445942851 589 GRRYALLVDQLIGQHQVVVKNLESNY----RKVPGISAATILGDGSVALIVDVSAL 640
Cdd:cd00588   81 DRKVGLVVDSVLGVLEVVIKDIEPPPdvgsSNAPGISGATILGDGRVVLILDVDKL 136
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 514-640 2.95e-28

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 109.98  E-value: 2.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  514 GMSVRVADEVFILPLNAVMESLQPREADLHPLAGG--ERVLEVRGEYLPIVELWKVFNVAGAKTEaTQGIVVILQSGGRR 591
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 445942851  592 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 640
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 7-99 6.90e-25

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 98.86  E-value: 6.90e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851     7 DFYQTFFDEADELLADMEQHLLVLQpEAPDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGEMQLNTD 86
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELE-KALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|...
gi 445942851    87 IINLFLETKDIMQ 99
Cdd:smart00073  80 LLDLLLELVDVLK 92
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 372-508 1.61e-23

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 95.79  E-value: 1.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   372 DPLTHLVRNSLDHGIELPEKRlaagknsvGNLILSAEHQGGNICIEVTDDGAGLnrerilakaasqgltvsenmsDDEVA 451
Cdd:smart00387   4 DRLRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGI---------------------PPEDL 54

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 445942851   452 MLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLT 508
Cdd:smart00387  55 EKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 5-103 5.93e-23

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 93.60  E-value: 5.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851   5 ISDFYQTFFDEADELLADMEQHLLVLQpeapDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLDEARRGeMQLN 84
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELE----DAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVT 75

                         90
                 ....*....|....*....
gi 445942851  85 TDIINLFLETKDIMQEQLD 103
Cdd:cd00088   76 PELIDLLLDALDALKAELE 94
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 263-324 1.69e-16

Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the homodimer interface of the signal transducing histidine kinase family.


Pssm-ID: 427045 [Multi-domain]  Cd Length: 66  Bit Score: 74.20  E-value: 1.69e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 445942851  263 SIRVAVEKVDQLINLVGELVITQSMLAQRSSEL----DPVNHGDLITSMGQLQRNARDLQESVMSI 324
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLERLeeygGDTLLEELKEALQQLDRLTRELQEAVMKI 66
CheY-binding pfam09078
CheY binding; Members of this family adopt a secondary structure consisting of an open-face ...
 161-223 1.09e-15

CheY binding; Members of this family adopt a secondary structure consisting of an open-face beta/alpha sandwich, with four antiparallel beta-strands and two alpha-helices. They bind to a corresponding domain on CheY, with subsequent phosphorylation of the CheY Asp57 residue, and activation of CheY, which then affects flagellar rotation.


Pssm-ID: 430396 [Multi-domain]  Cd Length: 63  Bit Score: 71.82  E-value: 1.09e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445942851  161 RIILSRLKAGEVDLLEEELGHLTTLNDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITF 223
Cdd:pfam09078   1 RIRLSGVSDKDVELLVEELGLLGEVLAQEQAGDSLSVWLETTVSEDDIIAVCCFVVDPDQIVI 63
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 371-508 2.64e-15

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 72.02  E-value: 2.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851  371 IDPLTHLVRNSLDHGIElpekrlAAGKNSVGNLILsaeHQGGNICIEVTDDGAGLNRERIlakaasqgltvsenmsddev 450
Cdd:pfam02518   3 ELRLRQVLSNLLDNALK------HAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDL-------------------- 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 445942851  451 aMLIFAPgFSTAEqVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLT 508
Cdd:pfam02518  54 -PRIFEP-FSTAD-KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 7-93 7.41e-14

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 67.38  E-value: 7.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851    7 DFYQTFFDEADELLADMEQHLlvlqpeapDAEQLNAIFRAAHSIKGGAGTFGFSVLQETTHLMENLLdeaRRGEMQLNTD 86
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL---REGELPLDPE 69


                  ....*..
gi 445942851   87 IINLFLE 93
Cdd:pfam01627  70 LLEALRD 76
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
338-508 1.05e-13

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 71.09  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 338 RLVRDLAGKLGKQVELTLVGSSTEL--DKSLIERIidpLTHLVRNSLDHGielPEKrlaagknsvGNLILSAEHQGGNIC 415
Cdd:COG2205  102 EELRPLAEEKGIRLELDLPPELPLVyaDPELLEQV---LANLLDNAIKYS---PPG---------GTITISARREGDGVR 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 416 IEVTDDGAGlnrerilakaasqgltvsenMSDDEVAMlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQ 495
Cdd:COG2205  167 ISVSDNGPG--------------------IPEEELER-IFER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEP 224

                        170
                 ....*....|...
gi 445942851 496 GTGTTIRILLPLT 508
Cdd:COG2205  225 GGGTTFTVTLPLA 237
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
338-508 7.64e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.94  E-value: 7.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 338 RLVRDLAGKLGKQVELTLVGSSTEL--DKSLIERIidpLTHLVRNSLDHGielpekrlAAGknsvGNLILSAEHQGGNIC 415
Cdd:COG0642  193 ELFRPLAEEKGIELELDLPDDLPTVrgDPDRLRQV---LLNLLSNAIKYT--------PEG----GTVTVSVRREGDRVR 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 416 IEVTDDGAGlnrerilakaasqgltvsenMSDDEVAMlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQ 495
Cdd:COG0642  258 ISVEDTGPG--------------------IPPEDLER-IFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEP 315

                        170
                 ....*....|...
gi 445942851 496 GTGTTIRILLPLT 508
Cdd:COG0642  316 GKGTTFTVTLPLA 328
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 338-508 7.82e-11

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 64.60  E-value: 7.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 338 RLVRDLAGKLGKQVELTLVGSSTEL--DKSLIERIidpLTHLVRNSLDhgielpekrlAAGKNsvGNLILSAEHQGGNIC 415
Cdd:COG5000  287 ALYEPALKEKDIRLELDLDPDLPEVlaDRDQLEQV---LINLLKNAIE----------AIEEG--GEIEVSTRREDGRVR 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 416 IEVTDDGAGLNRErILAKaasqgltvsenmsddevamlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQ 495
Cdd:COG5000  352 IEVSDNGPGIPEE-VLER--------------------IFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRP 405

                        170
                 ....*....|...
gi 445942851 496 GTGTTIRILLPLT 508
Cdd:COG5000  406 GGGTTFTIRLPLA 418
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 252-508 8.72e-10

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 60.97  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 252 REKTTRSSESTSIRVAVEKVDQLINLVGElvITQSMLA---QRSSELDPVnhgdlitsmgqlqrnarDLQESVMSIRmmp 328
Cdd:COG4191  168 RRRLEDEPDPEELREALERILEGAERAAE--IVRSLRAfsrRDEEEREPV-----------------DLNELIDEAL--- 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 329 meyvfsrypRLVRDLAGKLGKQVELTLVGS--STELDKSLIERIidpLTHLVRNSLDhgielpekrlAAGKNSVGNLILS 406
Cdd:COG4191  226 ---------ELLRPRLKARGIEVELDLPPDlpPVLGDPGQLEQV---LLNLLINAID----------AMEEGEGGRITIS 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 407 AEHQGGNICIEVTDDGAGLNRErILAKaasqgltvsenmsddevamlIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMG 486
Cdd:COG4191  284 TRREGDYVVISVRDNGPGIPPE-VLER--------------------IFEPFFTTKPVG---KGTGLGLSISYGIVEKHG 339

                        250       260
                 ....*....|....*....|..
gi 445942851 487 GHVEIQSKQGTGTTIRILLPLT 508
Cdd:COG4191  340 GRIEVESEPGGGTTFTITLPLA 361
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
340-508 2.33e-09

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 59.47  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 340 VRDLAGK-LGKQVELTLvgsstELDKSLIERIIDP------LTHLVRNSLDHGIELPEKRLAAGKnsVGNLILSAEHQGG 412
Cdd:COG3852  213 VLELLRAeAPKNIRIVR-----DYDPSLPEVLGDPdqliqvLLNLVRNAAEAMPEGGTITIRTRV--ERQVTLGGLRPRL 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 413 NICIEVTDDGAGLNRErILAKaasqgltvsenmsddevamlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEIQ 492
Cdd:COG3852  286 YVRIEVIDNGPGIPEE-ILDR--------------------IFEPFFTTKEK-----GTGLGLAIVQKIVEQHGGTIEVE 339

                        170
                 ....*....|....*.
gi 445942851 493 SKQGTGTTIRILLPLT 508
Cdd:COG3852  340 SEPGKGTTFRIYLPLE 355
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 363-506 2.97e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 59.93  E-value: 2.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 363 DKSLIERIIDPLTHLVRNSLDhgielpekrlAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaasqgltvs 442
Cdd:PRK11086 427 DEDQVHELITILGNLIENALE----------AVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDA---------- 486

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942851 443 enmsddevamlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:PRK11086 487 -----------IFDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 377-510 2.73e-08

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 56.40  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 377 LVRNSLDHgielpekrLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaasqgltvsenmsDDEVAMLIFA 456
Cdd:COG3290  289 LLDNAIEA--------VEKLPEEERRVELSIRDDGDELVIEVEDSGPGI---------------------PEELLEKIFE 339

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445942851 457 PGFSTAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLA 510
Cdd:COG3290  340 RGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
412-507 4.19e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 53.05  E-value: 4.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 412 GNICIEVTDDGAGLNRERILAkaasqgltvsenmsddevamlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEI 491
Cdd:PRK11360 532 GQVAVSIEDNGCGIDPELLKK---------------------IFDPFFTTKAK-----GTGLGLALSQRIINAHGGDIEV 585

                         90
                 ....*....|....*.
gi 445942851 492 QSKQGTGTTIRILLPL 507
Cdd:PRK11360 586 ESEPGVGTTFTLYLPI 601
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
237-507 4.64e-07

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 52.63  E-value: 4.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 237 VLKLAAEQAPTGRVEREKTTRSSestsIRVAVEKVDQLINLVGELvitqsmlaqrsseLDpvnhgdlitsMGQLQRNARD 316
Cdd:COG5002  182 SIRGYLELLLDGAADDPEERREY----LEIILEEAERLSRLVNDL-------------LD----------LSRLESGELK 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 317 LQESVMSIRMMpMEYVFSRYprlvRDLAGKlgKQVELTLVGSSTEL----DKSLIERIidpLTHLVRNSLDHGielPEKr 392
Cdd:COG5002  235 LEKEPVDLAEL-LEEVVEEL----RPLAEE--KGIELELDLPEDPLlvlgDPDRLEQV---LTNLLDNAIKYT---PEG- 300

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 393 laagknsvGNLILSAEHQGGNICIEVTDDGAGlnrerilakaasqgltvsenMSDDEVAMlIFAPgFSTAEQVT--DVSG 470
Cdd:COG5002  301 --------GTITVSLREEDDQVRISVRDTGIG--------------------IPEEDLPR-IFER-FYRVDKSRsrETGG 350

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 445942851 471 RGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPL 507
Cdd:COG5002  351 TGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
361-508 6.02e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 52.33  E-value: 6.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 361 ELDKSLIERIIDPLT--HLVRNSLDHGIElpekrlaaGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaasqg 438
Cdd:COG2972  326 EIDEELLDLLIPKLIlqPLVENAIEHGIE--------PKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEK------ 391

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942851 439 ltVSENMSDDEvamlifapgfstaeqvtdvSGRGVGMdvvkRNIQEM-------GGHVEIQSKQGTGTTIRILLPLT 508
Cdd:COG2972  392 --LLEELSSKG-------------------EGRGIGL----RNVRERlklyygeEYGLEIESEPGEGTTVTIRIPLE 443
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 411-506 1.31e-06

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 47.76  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 411 GGNICIEVTDDGAGLNRErILAKAasqgltvsenmsddevamliFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGHVE 490
Cdd:cd16919   45 GNYVCLEVSDTGSGMPAE-VLRRA--------------------FEPFFTTKEVG---KGTGLGLSMVYGFVKQSGGHLR 100

                         90
                 ....*....|....*.
gi 445942851 491 IQSKQGTGTTIRILLP 506
Cdd:cd16919  101 IYSEPGVGTTVRIYLP 116
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
516-640 1.92e-06

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 47.94  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 516 SVRVADEVFILPLNAVMESLQPREadLHPLAGGER----VLEVRGEYLPIVELWKVFNVAgAKTEATQGIVVILQSGGRR 591
Cdd:COG0835   12 TFRLGGERYAIPIEKVREILPLPP--ITPVPGAPPwvlgVINLRGRVVPVIDLRALLGLP-PTEDTERTRIIVLEVGGRV 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 445942851 592 YALLVDQLIGQHQVVVKNLESNYRKVPGISAATILG----DGSVALIVDVSAL 640
Cdd:COG0835   89 VGLLVDSVSGVVRIDPDDIEPPPELLSGGLAPFITGvaklDDRLILLLDLEKL 141
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 397-506 1.92e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 46.67  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 397 KNSVGNLILSAEHQGGnICIEVTDDGAGlNRERILAKAASQGLTVSENMSddevamlIFAPgFSTAEQVTDVSGRGVGMD 476
Cdd:cd16950    2 KRVLSNLVDNALRYGG-GWVEVSSDGEG-NRTRIQVLDNGPGIAPEEVDE-------LFQP-FYRGDNARGTSGTGLGLA 71

                         90       100       110
                 ....*....|....*....|....*....|
gi 445942851 477 VVKRNIQEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:cd16950   72 IVQRISDAHGGSLTLANRAGGGLCARIELP 101
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 377-506 4.18e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 45.74  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 377 LVRNSLDhgielpekRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaasqgltvsenmsDDEVAMLIFA 456
Cdd:cd16915    8 LIDNALD--------ALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGI---------------------APELRDKVFE 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 445942851 457 PGFSTAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:cd16915   59 RGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 411-507 1.15e-05

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 48.43  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 411 GGNICIEVTDdgagLNRERILAKAASQGLTVSENMSDdevamLIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVE 490
Cdd:COG5809  398 GGNITIETKA----EDDDKVVISVTDEGCGIPEERLK-----KLGEPFYTTKEK-----GTGLGLMVSYKIIEEHGGKIT 463

                         90
                 ....*....|....*..
gi 445942851 491 IQSKQGTGTTIRILLPL 507
Cdd:COG5809  464 VESEVGKGTTFSITLPI 480
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 338-508 1.26e-05

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 48.19  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 338 RLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDP------LTHLVRNSLDhgiELPekrlaagknSVGNLILSAEHQG 411
Cdd:COG5805  358 ELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDEnqikqvFINLIKNAIE---AMP---------NGGTITIHTEEED 425

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 412 GNICIEVTDDGAGLNRERiLAKaasqgltvsenmsddevamlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEI 491
Cdd:COG5805  426 NSVIIRVIDEGIGIPEER-LKK--------------------LGEPFFTTKEK-----GTGLGLMVSYKIIENHNGTIDI 479

                        170
                 ....*....|....*..
gi 445942851 492 QSKQGTGTTIRILLPLT 508
Cdd:COG5805  480 DSKVGKGTTFTITLPLS 496
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
338-507 1.43e-05

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 47.86  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 338 RLVRDLAGKLGKQVELTlVGSSTELDKSLIERIIDPLTHLVRNSLDhgielpekrlAAGKNsvGNLILSAEHQGGNICIE 417
Cdd:PRK10364 318 QLVSQDANSREIQLRFT-ANDTLPEIQADPDRLTQVLLNLYLNAIQ----------AIGQH--GVISVTASESGAGVKIS 384

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 418 VTDDGAGLNRERILAkaasqgltvsenmsddevamlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEIQSKQGT 497
Cdd:PRK10364 385 VTDSGKGIAADQLEA---------------------IFTPYFTTKAE-----GTGLGLAVVHNIVEQHGGTIQVASQEGK 438

                        170
                 ....*....|
gi 445942851 498 GTTIRILLPL 507
Cdd:PRK10364 439 GATFTLWLPV 448
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 363-506 3.14e-05

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 47.09  E-value: 3.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 363 DKSLIERIidpLTHLVRNSLDHGielpekrlaaGKNSVGNLILSAEHQGGNICIEVTDDGAGLN---RERilakaasqgl 439
Cdd:COG4251  391 DPTLLRQV---FQNLISNAIKYS----------RPGEPPRIEIGAEREGGEWVFSVRDNGIGIDpeyAEK---------- 447

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445942851 440 tvsenmsddevamlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:COG4251  448 --------------IFEI-FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 406-507 6.21e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 42.48  E-value: 6.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 406 SAEHQGGNICIEVTDDGAGLNRERILakaasqgltvsenmsddevamLIFAPgFSTAEQVT--DVSGRGVGMDVVKRNIQ 483
Cdd:cd16922   29 EEEEDGVQLRFSVEDTGIGIPEEQQA---------------------RLFEP-FSQADSSTtrKYGGTGLGLAISKKLVE 86

                         90       100
                 ....*....|....*....|....
gi 445942851 484 EMGGHVEIQSKQGTGTTIRILLPL 507
Cdd:cd16922   87 LMGGDISVESEPGQGSTFTFTLPL 110
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 416-507 8.02e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 42.02  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 416 IEVTDDGAGLNRErILAKaasqgltvsenmsddevamlIFAPGFSTAEQVTdvsGRGVGMDVVKRNIQEMGGHVEIQSKQ 495
Cdd:cd16943   38 IEVEDTGSGIDPE-ILGR--------------------IFDPFFTTKPVGE---GTGLGLSLSYRIIQKHGGTIRVASVP 93

                         90
                 ....*....|..
gi 445942851 496 GTGTTIRILLPL 507
Cdd:cd16943   94 GGGTRFTIILPI 105
PRK13557 PRK13557
histidine kinase; Provisional
 237-518 1.31e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 45.05  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 237 VLKLAAEqAPTGRVERekTTRSSEStsIRVAVEKVDQLinlvgelviTQSMLA-QRSSELD--PVNHGDLITSMGQLQRN 313
Cdd:PRK13557 187 VIQAALS-HPDADRGR--MARSVEN--IRAAAERAATL---------TQQLLAfARKQRLEgrVLNLNGLVSGMGELAER 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 314 ArdlqesvmsirmmpmeyvfsryprlvrdlagkLGKQVELtlvgsSTELDKSLIERIIDP------LTHLVRNSLDHGIE 387
Cdd:PRK13557 253 T--------------------------------LGDAVTI-----ETDLAPDLWNCRIDPtqaevaLLNVLINARDAMPE 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 388 LPEKRLAAGKNSVGNLILSAEHQ---GGNICIEVTDDGAGLNRErILAKaasqgltVSEnmsddevamlifaPGFSTAEQ 464
Cdd:PRK13557 296 GGRVTIRTRNVEIEDEDLAMYHGlppGRYVSIAVTDTGSGMPPE-ILAR-------VMD-------------PFFTTKEE 354

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 445942851 465 VtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVR 518
Cdd:PRK13557 355 G---KGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEP 405
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 400-506 1.95e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 41.12  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 400 VGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaasqgltvsenmsddevamlIFAPGFSTAEQVTDVSGRGVGMDVVK 479
Cdd:cd16948   24 GGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPR---------------------VFDKGFTGENGRNFQESTGMGLYLVK 82

                         90       100
                 ....*....|....*....|....*..
gi 445942851 480 RNIQEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:cd16948   83 KLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 374-506 5.25e-04

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 41.17  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 374 LTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHqggnICIEVTDDGAGLNReRILAKAASQGLTVSENMSDDEVAML 453
Cdd:cd16929   48 LFELLKNAMRATVESHGDDSDDLPPIKVTVAKGDED----LTIKISDRGGGIPR-EDLARLFSYMYSTAPQPSLDDFSDL 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 445942851 454 IfapgfsTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:cd16929  123 I------SGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 404-506 6.50e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 39.83  E-value: 6.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 404 ILSAEHQGGNICIEVTDDGAGLNRERIlakaasqgltvsenmsddevamlifapGFSTAEQVTDVS-GRGVGMDVVKRNI 482
Cdd:cd16944   32 IRVEADQDGRIVLIVCDNGKGFPREMR---------------------------HRATEPYVTTRPkGTGLGLAIVKKIM 84

                         90       100
                 ....*....|....*....|....
gi 445942851 483 QEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:cd16944   85 EEHGGRISLSNREAGGACIRIILP 108
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 470-506 7.86e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 39.23  E-value: 7.86e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 445942851 470 GRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 506
Cdd:cd16921   69 GTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
281-508 1.09e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 41.14  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 281 LVITQSMLAQRSSELDPVNHGDLITSMGQLQRNA-RDLQESVMSIRMMPMEYV--FSRYPRLVRDLAGKLGKQVELTLVG 357
Cdd:COG4585   71 AIKLQLEAARRLLDADPEAAREELEEIRELAREAlAELRRLVRGLRPPALDDLglAAALEELAERLLRAAGIRVELDVDG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 358 SSTELDKSL---IERIIdplTHLVRNSLDHGielpekrlaagknSVGNLILSAEHQGGNICIEVTDDGAGLNRERilaka 434
Cdd:COG4585  151 DPDRLPPEVelaLYRIV---QEALTNALKHA-------------GATRVTVTLEVDDGELTLTVRDDGVGFDPEA----- 209

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 445942851 435 asqgltvsenmsddevamlifapgfstaeqvtdVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLT 508
Cdd:COG4585  210 ---------------------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 374-507 2.50e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 37.69  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 374 LTHLVRNSLDHgielpekrlaagknSVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaasqgltvsenmSDDEVAMl 453
Cdd:cd16949    5 LENVLRNALRY--------------SPSKILLDISQDGDQWTITITDDGPGV--------------------PEDQLEQ- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 445942851 454 IFAPGFSTAEQVTDVS-GRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPL 507
Cdd:cd16949   50 IFLPFYRVDSARDRESgGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
 518-640 3.55e-03

CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. CheW interacts with the histidine kinase CheA, most likely with the related regulatory domain of CheA. CheW is proposed to form signalling arrays together with CheA and the methyl-accepting chemotaxis proteins (MCPs), which are involved in response modulation.


Pssm-ID: 238374  Cd Length: 140  Bit Score: 38.32  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 518 RVADEVFILPLNAVMESLQPREADLHPLAGG--ERVLEVRGEYLPIVELWKVFNVAGAKTEAtQGIVVILQSGGRRYALL 595
Cdd:cd00732    8 RLGDEEYGIPIMQVREILKPTPITPIPNAPPyvLGVINLRGRIVPVIDLRKRLGLPPAEDTK-NTRIIVVEVGDQVVGLL 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 445942851 596 VDQLIGQHQVVVKNLESNYRKVPGISAATILG----DGSVALIVDVSAL 640
Cdd:cd00732   87 VDSVSEVLRLSTDDIQPPPPVLSDINAKFIRGvvklEGRLLILLDLDKI 135
PRK15347 PRK15347
two component system sensor kinase;
401-508 4.13e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.40  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 401 GNLILSAEHQGGNICIEVTDDGAGLNRERILAkaasqgltvsenmsddevamlIFAPGFSTAeqvTDVSGRGVGMDVVKR 480
Cdd:PRK15347 532 GGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQ---------------------IFTPFYQAD---THSQGTGLGLTIASS 587

                         90       100
                 ....*....|....*....|....*...
gi 445942851 481 NIQEMGGHVEIQSKQGTGTTIRILLPLT 508
Cdd:PRK15347 588 LAKMMGGELTLFSTPGVGSCFSLVLPLN 615
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 370-505 4.95e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 37.05  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445942851 370 IIDPLTHLVRNSLDhgielpekrlAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLnrerilakaasqgltvsenmsDDE 449
Cdd:cd16976    1 IQQVLMNLLQNALD----------AMGKVENPRIRIAARRLGGRLVLVVRDNGPGI---------------------AEE 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445942851 450 VAMLIFAPGFSTaeqvTDV-SGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILL 505
Cdd:cd16976   50 HLSRVFDPFFTT----KPVgKGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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